Literature DB >> 23382

Characterization of the ionizable groups interacting with anionic allosteric effectors of human hemoglobin.

E Bucci, A Salahuddin, J Bonaventura, C Bonaventura.   

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Year:  1978        PMID： 23382

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  5 in total

1.  Liganded hemoglobin structural perturbations by the allosteric effector L35.

Authors:  Qiuying Chen; Iraj Lalezari; Ronald L Nagel; Rhoda Elison Hirsch
Journal:  Biophys J       Date:  2004-12-30       Impact factor: 4.033

2.  Species differences in the binding of compounds designed to fit a site of known structure in adult human haemoglobin.

Authors:  C R Beddell; P J Goodford; D K Stammers; R Wootton
Journal:  Br J Pharmacol       Date:  1979-03       Impact factor: 8.739

3.  Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin.

Authors:  Xiang-jin Song; Virgil Simplaceanu; Nancy T Ho; Chien Ho
Journal:  Biochemistry       Date:  2008-04-01       Impact factor: 3.162

4.  Interaction of organic phosphates with bovine hemoglobin. I. Oxylabile and phosphate-labile proton binding.

Authors:  P M Breepoel; F Kreuzer; M Hazevoet
Journal:  Pflugers Arch       Date:  1981-03       Impact factor: 3.657

5.  Mellitate: A multivalent anion with extreme charge density causes rapid aggregation and misfolding of wild type lysozyme at neutral pH.

Authors:  Grzegorz Ścibisz; Robert Dec; Wojciech Dzwolak
Journal:  PLoS One       Date:  2017-10-30       Impact factor: 3.240
  5 in total

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